ID   SOL5_ALTSO              Reviewed;         515 AA.
AC   D7UQ40;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   25-MAY-2022, entry version 43.
DE   RecName: Full=Bifunctional solanapyrone synthase {ECO:0000303|PubMed:20486243};
DE            EC=1.1.3.42 {ECO:0000269|PubMed:18256508, ECO:0000269|PubMed:20486243, ECO:0000269|PubMed:9659400};
DE            EC=5.5.1.20 {ECO:0000269|PubMed:18256508, ECO:0000269|PubMed:20486243, ECO:0000269|PubMed:9659400};
DE   AltName: Full=FAD-dependent monooxygenase sol5 {ECO:0000305};
DE   AltName: Full=Prosolanapyrone-II oxidase;
DE   AltName: Full=Prosolanapyrone-III cycloisomerase;
DE   AltName: Full=Solanapyrone biosynthesis protein 5 {ECO:0000303|PubMed:20486243};
DE   Flags: Precursor;
GN   Name=sol5;
OS   Alternaria solani.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC   Alternaria sect. Porri.
OX   NCBI_TaxID=48100;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=20486243; DOI=10.1002/cbic.201000173;
RA   Kasahara K., Miyamoto T., Fujimoto T., Oguri H., Tokiwano T., Oikawa H.,
RA   Ebizuka Y., Fujii I.;
RT   "Solanapyrone synthase, a possible Diels-Alderase and iterative type I
RT   polyketide synthase encoded in a biosynthetic gene cluster from Alternaria
RT   solani.";
RL   ChemBioChem 11:1245-1252(2010).
RN   [2]
RP   PROTEIN SEQUENCE OF 26-42, FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=18256508; DOI=10.1271/bbb.70600;
RA   Katayama K., Kobayashi T., Chijimatsu M., Ichihara A., Oikawa H.;
RT   "Purification and N-terminal amino acid sequence of solanapyrone synthase,
RT   a natural Diels-Alderase from Alternaria solani.";
RL   Biosci. Biotechnol. Biochem. 72:604-607(2008).
RN   [3]
RP   CATALYTIC ACTIVITY, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=9659400; DOI=10.1016/s0167-4838(98)00040-5;
RA   Katayama K., Kobayashi T., Oikawa H., Honma M., Ichihara A.;
RT   "Enzymatic activity and partial purification of solanapyrone synthase:
RT   first enzyme catalyzing Diels-Alder reaction.";
RL   Biochim. Biophys. Acta 1384:387-395(1998).
CC   -!- FUNCTION: Bifunctional solanapyrone synthase; part of the gene cluster
CC       that mediates the biosynthesis of the phytotoxin solanapyrone, a causal
CC       agent of early blight disease of potato and tomato (PubMed:20486243).
CC       The prosolanapyrone synthase sol1 is a polyketide synthase that
CC       produces the octaketide desmethylprosolanapyrone I via sequential
CC       condensations of 7 malonyl-CoA units with one acetyl-CoA unit, and one
CC       methylation step (PubMed:20486243). The octaketide backbone is further
CC       methylated by the sol2 O-methyltransferase to yield prosolanapyrone I
CC       (PubMed:20486243). Prosolanapyrone I is hydroxylated to prosolanapyrone
CC       II by the cytochrome P450 monooxygenase sol6 (PubMed:20486243). The
CC       solanapyrone synthase sol5 then catalyzes the oxidation of
CC       prosolanapyrone II and the subsequent Diels Alder cycloisomerization of
CC       the product prosolanapyrone III to solanapyrones A and D
CC       (PubMed:9659400, PubMed:18256508). Solanapyrones A and D are then
CC       converted into solanapyrones B and E, respectively, by the sol3
CC       dehydrogenase (PubMed:20486243). {ECO:0000269|PubMed:18256508,
CC       ECO:0000269|PubMed:20486243, ECO:0000269|PubMed:9659400}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O2 + prosolanapyrone II = H2O2 + prosolanapyrone III;
CC         Xref=Rhea:RHEA:31679, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:38238, ChEBI:CHEBI:63164; EC=1.1.3.42;
CC         Evidence={ECO:0000269|PubMed:18256508, ECO:0000269|PubMed:20486243,
CC         ECO:0000269|PubMed:9659400};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=prosolanapyrone III = (-)-solanapyrone A;
CC         Xref=Rhea:RHEA:31683, ChEBI:CHEBI:38229, ChEBI:CHEBI:63164;
CC         EC=5.5.1.20; Evidence={ECO:0000269|PubMed:18256508,
CC         ECO:0000269|PubMed:20486243, ECO:0000269|PubMed:9659400};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=16 uM for Prosolanapyrone II {ECO:0000269|PubMed:9659400};
CC   -!- PATHWAY: Phytotoxin biosynthesis. {ECO:0000269|PubMed:18256508,
CC       ECO:0000269|PubMed:20486243, ECO:0000269|PubMed:9659400}.
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DR   EMBL; AB514562; BAJ09785.1; -; Genomic_DNA.
DR   AlphaFoldDB; D7UQ40; -.
DR   SMR; D7UQ40; -.
DR   KEGG; ag:BAJ09785; -.
DR   BRENDA; 1.1.3.42; 269.
DR   BRENDA; 5.5.1.20; 269.
DR   SABIO-RK; D7UQ40; -.
DR   PHI-base; PHI:3347; -.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.465.10; -; 1.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; SSF56176; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; FAD; Flavoprotein; Glycoprotein; Isomerase;
KW   Oxidoreductase; Signal; Virulence.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000269|PubMed:18256508"
FT   CHAIN           26..515
FT                   /note="Bifunctional solanapyrone synthase"
FT                   /id="PRO_0000416192"
FT   DOMAIN          91..261
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT   MOD_RES         128
FT                   /note="Pros-8alpha-FAD histidine"
FT                   /evidence="ECO:0000250|UniProtKB:P08159"
FT   CARBOHYD        66
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        274
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        355
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   515 AA;  55994 MW;  7BCCBD564458484D CRC64;
     MRLIILNLLS LGITPSVVGH SGPHRQETQN LNNFLESNAI NPAAINGETR HTGGVHLACA
     ILEASNQTAV VFPSDGELYT QIDKAHASAT APKNPACIYT PNDVKGVSLG VKVATFVQAK
     FAIRSGGHSP MEYFANIDGG VLISLAGIKT LEYNADTQTQ RSGFGNLWQD VYRHVNAQGR
     TVVGGRTGSV GLALTLGGGL SHFSNAYGWA AQNVLSYEMV LADGSIVIAS EEENSDLYFA
     VKAGANNFGI VTHIVQRTYP LGKIWGGSMI FPGNASAQFM AALADYQAKG QLDKKSAILP
     YVGLIADAVV AQFSYLEPVE RPEAFEAFYD IPVIQDLTQV WDTFAAMVTA PIPYNMTRFS
     YATTDLLYDK EAYLEIERIC HKYIPRMRKL EGGDIMLMPQ PISVSMVGEA RARGSDPMGV
     ADQPQLWFVV SSGWNLAQDD AEAESIMLDA LAEVEEYTKS RALHLPFYFL NDAFSTQMPL
     QSYGAVTYGK LQAASRKYDP TRVFQELVPG GFKLV